MolNFT v1 · #127248 · protein
Thermophilic archaeal branched-chain amino acid transaminases from geoglobus acetivorans and archaeoglobus fulgidus: biochemical and structural characterisation
5MR0: “Thermophilic archaeal branched-chain amino acid transaminases from geoglobus acetivorans and archaeoglobus…”. X-ray diffraction, 3 ligands (PXG, TAM, CL). MolNFT v1 #127248 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5MR0
- Type
- protein
- Length
- 1,723 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O29329
- Ligands
- PXG, TAM, CL
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, F | — | protein | 287 | — | O29329 |
| B, C | — | protein | 286 | — | O29329 |
| D | — | protein | 290 | — | O29329 |
Ligands and binding sites
- PXG · 3-[O-phosphonopyridoxyl]--amino-benzoic acid · ligand · 5 copies · chains A, B, C, D, E, F
- TAM · Tris(hydroxyethyl)aminomethane · ligand · 2 copies · chains B, D, E, A, C, F
- CL · Chloride ion · ion · 9 copies · chains A, B, C, E, D, F
- PEG · Di(hydroxyethyl)ether · additive · 9 copies · chains A, B, D, C
- EDO · 1,2-ethanediol · additive · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5MR0 · Thermophilic archaeal branched-chain amino acid transaminases from Geoglobus acetivorans… · the same entry in another collection · chain F against F, TM-score 1.00
- O29329 · AlphaFold monomer V2.0 prediction for putative branched-chain-amino- acid… · a predicted model of the same protein · chain B against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O29329
- Elsewhere: RCSB PDB 5MR0 · PDBe 5MR0 · UniProt O29329
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